Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9FMT1 (LEU33_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase 3, chloroplastic

Short name=3-IPM-DH 3
Short name=IMDH 3
EC=1.1.1.85
Alternative name(s):
Beta-IPM dehydrogenase 3
Gene names
Name:IMDH3
Ordered Locus Names:At5g14200
ORF Names:MUA22.20
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FMT1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Chloroplast Potential
Chain38 – 4093723-isopropylmalate dehydrogenase 3, chloroplastic
PRO_0000014455

Regions

Nucleotide binding120 – 13314NAD By similarity
Nucleotide binding326 – 33813NAD By similarity

Sites

Metal binding2681Magnesium or manganese By similarity
Metal binding2921Magnesium or manganese By similarity
Metal binding2961Magnesium or manganese By similarity
Binding site1401Substrate By similarity
Binding site1501Substrate By similarity
Binding site1781Substrate By similarity
Binding site2681Substrate By similarity
Site1851Important for catalysis By similarity
Site2361Important for catalysis By similarity

Amino acid modifications

Modified residue741Phosphoserine Ref.4

Experimental info

Sequence conflict2511T → A in AAL67125. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 471293D4C3FB55DD

FASTA40944,162
        10         20         30         40         50         60 
MAAFLQTNIS LNAIKIVPGK YSSLTDHQFR APYRIRCAAA SPGKKRYNIA LLPGDGIGPE 

        70         80         90        100        110        120 
VISVAKNVLQ KAGSLEGLEF DFKEMPVGGA ALDLVGVPLP EETFTAAKLS DAILLGAIGG 

       130        140        150        160        170        180 
YKWDKNEKHL RPEMALFYLR RDLKVFANLR PATVLPQLVD ASTLKKEVAE GVDMMIVREL 

       190        200        210        220        230        240 
TGGIYFGEPR GITINENGEE VGVSTEIYAA HEIDRIARVA FETARKRRGK LCSVDKANVL 

       250        260        270        280        290        300 
DASILWRKRV TALASEYPDV ELSHMYVDNA AMQLIRDPKQ FDTIVTNNIF GDILSDEASM 

       310        320        330        340        350        360 
ITGSIGMLPS ASLGESGPGL FEPIHGSAPD IAGQDKANPL ATILSAAMLL KYGLGEEKAA 

       370        380        390        400 
KRIEDAVVDA LNKGFRTGDI YSPGNKLVGC KEMGEEVLKS VESKVPATV 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007650 Genomic DNA. Translation: BAB08299.1.
CP002688 Genomic DNA. Translation: AED91997.1.
AY074587 mRNA. Translation: AAL67125.1.
IPIIPI00548301.
RefSeqNP_196924.1. NM_121424.5.
UniGeneAt.23937.
At.6515.

3D structure databases

ProteinModelPortalQ9FMT1.
SMRQ9FMT1. Positions 45-402.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9FMT1.

Proteomic databases

PRIDEQ9FMT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G14200.1; AT5G14200.1; AT5G14200.
GeneID831270.
GenomeReviewsGene locus AT5G14200 in contig BA000015_GR.
KEGGath:AT5G14200.
NMPDRfig|3702.1.peg.23549.

Organism-specific databases

TAIRAt5g14200.

Phylogenomic databases

GeneTreeEPGT00050000013531.
HOGENOMHBG518924.
InParanoidQ9FMT1.
OMAAAMMLRF.
PhylomeDBQ9FMT1.
ProtClustDBPLN02329.

Enzyme and pathway databases

BioCycARA:AT5G14200-MONOMER.
MetaCyc:AT5G14200-MONOMER.

Gene expression databases

GenevestigatorQ9FMT1.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK00052.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF13. IPMDH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. LeuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU33_ARATH
AccessionPrimary (citable) accession number: Q9FMT1
Secondary accession number(s): Q8VXU4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families